Cat: IPD-X32033

Recombinant Others LASB Protein (P. pastoris),His

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Analytical Data

  • Gene name

    LASB

  • 简介

    LASB proteins are multifunctional enzymes that exhibit broad substrate specificity by cleaving host elastin, collagen, IgG, multiple complement components, and endogenous proaminopeptidases. Furthermore, LASB exhibits autocatalytic activity in processing its own propeptide and plays a role in processing the propeptide of chitin-binding protein (cbpD). LASB Protein, Pseudomonas aeruginosa (P. pastoris, His) is the recombinant LASB protein, expressed by P. pastoris , with N-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    lasB; Neutral metalloproteinase PAE Pseudolysin Cleaved into the following chain: Pro-elastase;

  • Species

    Others

  • Source

    P. pastoris

  • Tag

    N-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P14756

  • Expression Region

    A198-L498

  • AA Sequence

    AEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCPSAL

  • Protein Length

    Full Length of Mature Protein

  • Molecular Weight

    68 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

The study of LASB (Lipid-binding and membrane-targeting proteins) recombinant proteins has gained significant importance in the field of molecular biology and biotechnology due to their essential roles in various cellular processes. LASB proteins are known to interact with lipid membranes, playing critical roles in signaling pathways, membrane trafficking, and cellular responses to environmental changes. The ability to express LASB proteins recombinantly allows researchers to investigate their structure-function relationships, elucidate their mechanisms of action, and explore their potential applications. Recombinant LASB proteins can be produced in various expression systems, facilitating large-scale production and functional assays. Moreover, understanding the interaction mechanisms of LASB proteins with lipids and membranes can lead to insights into disease mechanisms, particularly in conditions where membrane dynamics are altered, such as cancer and neurodegenerative diseases. The ongoing research aims not only to map the functional landscapes of these proteins but also to develop novel therapeutic strategies targeting LASB-related pathways, thus highlighting their relevance in both basic and applied biosciences. This area of research is rapidly evolving, with advancements in techniques such as structural biology and biophysics making it possible to obtain detailed information about LASB proteins, further driving interest in their characterization and potential exploitation in biotechnology and medicine.

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